Differential Expression of the Vegetative and Spore‐Bound Hydrophobins of <i>Trichoderma Reesei</i> Cloning and Characterization of the <i>Hfb2</i> Gene

Nakari-Setälä, Tiina; Aro, Nina; Ilmén, Marja; Muñoz, Gastón; Kalkkinen, Nisse; Penttilä, Merja

doi:10.1111/j.1432-1033.1997.00415.x

Cited by 98 publications

(104 citation statements)

References 46 publications

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“…Trifluoroacetic acid, ethanol, acetonitrile, and methanol from Merck were used as solvents. The hydrophobins HFBI and HFBII from H. jecorina (ϭ T. reesei) were used as reference proteins and purified by two-phase separation and reverse-phase high-performance liquid chromatography purification as described previously (29). Microbial strains and cultivations.…”

Section: Methodsmentioning

confidence: 99%

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Differential Regulation and Posttranslational Processing of the Class II Hydrophobin Genes from the Biocontrol FungusHypocrea atroviridis

Mikus

Lóránt

Neuhof³

et al. 2009

Appl Environ Microbiol

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Hydrophobins are small extracellular proteins, unique to and ubiquitous in filamentous fungi, which mediate interactions between the fungus and environment. The mycoparasitic fungus Hypocrea atroviridis has recently been shown to possess 10 different class II hydrophobin genes, which is a much higher number than that of any other ascomycete investigated so far. In order to learn the potential advantage of this hydrophobin multiplicity for the fungus, we have investigated their expression patterns under different physiological conditions (e.g., vegetative growth), various conditions inducing sporulation (light, carbon starvation, and mechanical injury-induced stress), and confrontation with potential hosts for mycoparasitism. The results show that the 10 hydrophobins display different patterns of response to these conditions: one hydrophobin (encoded by hfb-2b) is constitutively induced under all conditions, whereas other hydrophobins were formed only under conditions of carbon starvation (encoded by hfb-1c and hfb-6c) or light plus carbon starvation (encoded by hfb-2c, hfb-6a, and hfb-6b). The hydrophobins encoded by hfb-1b and hfb-5a were primarily formed during vegetative growth and under mechanical injury-provoked stress. hfb-22a was not expressed under any conditions and is likely a pseudogene. None of the 10 genes showed a specific expression pattern during mycoparasitic interaction. Most, but not all, of the expression patterns under the three different conditions of sporulation were dependent on one or both of the two blue-light regulator proteins BLR1 and BLR2, as shown by the use of respective loss-of-function mutants. Matrix-assisted laser desorption ionization-time of flight mass spectrometry of mycelial solvent extracts provided sets of molecular ions corresponding to HFB-1b, HFB-2a, HFB-2b, and HFB-5a in their oxidized and processed forms. These in silico-deduced sequences of the hydrophobins indicate cleavages at known signal peptide sites as well as additional N-and C-terminal processing. Mass peaks observed during confrontation with plant-pathogenic fungi indicate further proteolytic attack on the hydrophobins. Our study illustrates both divergent and redundant functions of the 10 hydrophobins of H. atroviridis.

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Section: Methodsmentioning

confidence: 99%

“…In Hypocrea jecorina (ϭ Trichoderma reesei), two major class II hydrophobins (HFB-1 and HFB-2) have been studied in detail (4) and shown to be formed under different physiological conditions (29). However, the genome sequence of H. jecorina contains six class II hfb genes (27), and the roles of HFB-3, HFB-4, HFB-5, and HFB-6 are yet unknown.…”

mentioning

confidence: 99%

Differential Regulation and Posttranslational Processing of the Class II Hydrophobin Genes from the Biocontrol FungusHypocrea atroviridis

Mikus

Lóránt

Neuhof³

et al. 2009

Appl Environ Microbiol

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“…The effect of hydrophobins on beer foam stability was studied by adding 0.1, 1 and 10 µg of the RP-HPLC purified HFBI 25 and HFBII 24 hydrophobins from T. reesei D75 into 0.33 L of bottled beer. The beer bottles were inverted once and the foam stability was measured using the NIBEM foam stability apparatus Model B (Haffmans BV Venlo, Holland) according to the manufacturer's instructions.…”

Section: Beer Foam Stabilitymentioning

confidence: 99%

“…Protein concentrations of the purified hydrophobin samples were determined using BC Assay Protein Determination Kit (Uptima, France) or BCA Protein Assay Reagent Kit (Pierce, Rockford, USA). In addition, a concentration of T. reesei hydrophobin samples was determined from the HPLC-chromatogram by using known amounts of the purified hydrophobins HFBI 25 or HFBII 24 as a standard. Partial N-terminal amino acid sequences of the purified proteins were determined by degradative Edman chemistry in the Protein Chemistry Laboratory of the Institute of Biotechnology, Finland 14 .…”

Section: Protein Analysesmentioning

confidence: 99%

Fungal Hydrophobins as Predictors of the Gushing Activity of Malt

Sarlin

Nakari-Setälä

Penttilä

et al. 2005

Journal of the Institute of Brewing

101

110

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Fungal infection of barley and malt, particularly by strains of the genus Fusarium, is known to be a direct cause of beer gushing. We have shown previously that small fungal proteins, hydrophobins, isolated from strains of the genera Fusarium, Nigrospora and Trichoderma act as gushing factors in beer. A hydrophobin concentration as low as 0.003 ppm was sufficient to induce gushing. The gushing-inducing abilities of the isolated hydrophobins varied probably due to their structural differences. The hydrophobins did not affect beer foam stability. A correlation was observed between the hydrophobin level analyzed by the hydrophobin ELISA developed and the gushing potential of malt. The risk of gushing was found to increase with hydrophobin concentrations above 250 µg/g malt. The levels of hydrophobin and the Fusarium mycotoxin deoxynivalenol (DON) in malts were not correlated which indicated that the formation of those two fungal metabolites may not be linked. Furthermore, we did not observe a correlation between the DON content and the gushing potential of the malt studied. Our observations suggest that the accuracy of predicting gushing could be improved by measuring the amount of the actual gushing factors, hydrophobins, in barley or malt.

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“…The quantitative composition of monomeric mixtures obtained depends on the method, but consists mostly of long-chain (16-24 carbon atoms) aliphatic dicarboxylic acids, ω-hydroxy fatty acids, very long chain (20)(21)(22)(23)(24)(25)(26)(27)(28)(29)(30) carbons) fatty acids, fatty alcohols, and glycerol together with a small amount of aromatic compounds such as coumaric and ferulic acids (1)(2)(3)(4)(5). The distribution of the individual suberin monomeric components and compound classes varies between different plant species and parts of plants.…”

Section: Introductionmentioning

confidence: 99%

Suberin of Potato (Solanum tuberosum Var. Nikola): Comparison of the Effect of Cutinase CcCut1 with Chemical Depolymerization

Järvinen¹,

Silvestre²,

Holopainen³

et al. 2009

J. Agric. Food Chem.

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Chemical and enzymatic depolymerizations of suberin isolated from potato peel (Solanum tuberosum var. Nikola) were performed under various conditions. Enzymatic hydrolysis with cutinase CcCut1 and chemical methanolysis with NaOMe of suberin yielded monomeric fragments, which were identified as TMS derivatives with GC-MS and GC-FID. The solid, hydrolysis-resistant residues were analyzed with solid state 13 C CPMAS NMR, FT-IR, and microscopic methods. Methanolysis released more CHCl 3 -soluble material than the cutinase treatment when determined gravimetrically. Interestingly, cutinase-catalyzed hydrolysis produced higher proportions of aliphatic monomers than hydrolysis with the NaOMe procedure when analyzed by GC in the form of TMS derivatives. Monomers released by the two methods were mainly R,ω-dioic acids and ω-hydroxy acids, but the ratios of the detected monomers were different, at 40.0 and 32.7% for methanolysis and 64.6 and 8.2% for cutinase, respectively. Thus, cutinase CcCut1 showed higher activity toward ester bonds of R,ω-dioic acids than toward the bonds of ω-hydroxy acids. The most abundant monomeric compounds were octadec-9-ene-1,18-dioic acid and 18-hydroxyoctadec-9-enoic acid, which accounted for ca. 37 and 28% of all monomers, respectively. The results of the analyses of the chemical and enzymatic hydrolysis products were supported by the spectroscopic analyses with FT-IR and CPMAS 13 C NMR together with the analysis of the microstructures of the hydrolysis residues by light and confocal microscopy.

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Differential Expression of the Vegetative and Spore‐Bound Hydrophobins of Trichoderma Reesei Cloning and Characterization of the Hfb2 Gene

Cited by 98 publications

References 46 publications

Differential Regulation and Posttranslational Processing of the Class II Hydrophobin Genes from the Biocontrol FungusHypocrea atroviridis

Differential Regulation and Posttranslational Processing of the Class II Hydrophobin Genes from the Biocontrol FungusHypocrea atroviridis

Fungal Hydrophobins as Predictors of the Gushing Activity of Malt

Suberin of Potato (Solanum tuberosum Var. Nikola): Comparison of the Effect of Cutinase CcCut1 with Chemical Depolymerization

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